期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 139, 期 23, 页码 8013-8021出版社
AMER CHEMICAL SOC
DOI: 10.1021/jacs.7b03812
关键词
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资金
- Office of Science, Office of Basic Energy Sciences
- Division of Chemical Sciences, Geosciences, and Bioscience of the U.S. Department of Energy at Lawrence Berkeley National Laboratory [DE-AC02-05CH11231]
- NSF GRFP [DGE 1106400]
This study offers a detailed mechanistic investigation of hostguest encapsulation behavior in a new enzyme-mimetic metal-ligand host and provides the first observation of a conformational selection mechanism (as opposed to induced fit) in a supramolecular system. The Ga4L4 host described features a C-3-symmetric ligand motif with meta-substituted phenyl spacers, which enables the host to initially self-assemble into an S-4-symmetric structure and then subsequently isomerize to a T-symmetric tetrahedron for better accommodation of a sufficiently large guest. Selective inversion recovery H-1 NMR studies provide structural insights into the self-exchange behaviors of the host and the guest individually in this dynamic system. Kinetic analysis of the encapsulation-isomerization event revealed that increasing the concentration of guest inhibits the rate of host-guest relaxation, a key distinguishing feature of conformational selection. A comprehensive study of this simple enzyme mimic provides insight into analogous behavior in biophysics and enzymology and aims to inform the design of efficient self-assembled microenvironment catalysts.
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